一般描述
Recognizes N- and C-terminal HSV fusion proteins.
免疫原
synthetic peptide corresponding to amino acids 290−300 of glycoprotein-D precursor, an envelop component of herpes simplex virus.
应用
Anti-HSV antibody was used to expand the repertoire of plasmids for PCR-mediated epitope tagging in yeast.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Chromatin immunoprecipitation (1 paper)
Western Blotting (1 paper)
Chromatin immunoprecipitation (1 paper)
Western Blotting (1 paper)
生化/生理作用
Anti-HSV is developed in rabbits using a synthetic peptide (K-QPELAPEDPED) conjugated to KLH via the N-terminal lysine. The peptide corresponds to amino acids 290-300 of Glycoprotein D precursor which is an envelope component of herpes simplex virus. Anti-HSV antibody reacts specifically with HSV tagged fusion proteins, using immunoblotting and immunoprecipitation techniques.
外形
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide.
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WGK
nwg
闪点(°F)
Not applicable
闪点(°C)
Not applicable
法规信息
含少量动物源组分生物产品
常规特殊物品
Obstetrical roundabout.
H E Cudby
Midwives chronicle, 91(1089), 301-301 (1978-10-01)
Expanding the repertoire of plasmids for PCR-mediated epitope tagging in yeast
Moqtaderi Z, Struhl K
Yeast, 4, 287-292 (2008)
Mitchell A Ellison et al.
Nucleic acids research, 51(10), 4814-4830 (2023-03-18)
The Paf1 complex (Paf1C) is a conserved transcription elongation factor that regulates transcription elongation efficiency, facilitates co-transcriptional histone modifications, and impacts molecular processes linked to RNA synthesis, such as polyA site selection. Coupling of the activities of Paf1C to transcription
Christine E Cucinotta et al.
Nucleic acids research, 47(16), 8410-8423 (2019-06-22)
The nucleosome core regulates DNA-templated processes through the highly conserved nucleosome acidic patch. While structural and biochemical studies have shown that the acidic patch controls chromatin factor binding and activity, few studies have elucidated its functions in vivo. We employed
P O Olins et al.
Current opinion in biotechnology, 4(5), 520-525 (1993-10-01)
Recent advances in protein expression in E. coli have focused primarily on the enhancement of protein quality. Problems in mRNA translation such as inefficient initiation, mistranslation, frame-shifting and frame-hopping can often be addressed by altering heterologous gene-coding sequences. Fusion technology
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